Isoforms of human O-GlcNAcase show distinct catalytic efficiencies

  title={Isoforms of human O-GlcNAcase show distinct catalytic efficiencies},
  author={J. Li and Cai-luan Huang and L. Zhang and L. Lin and Z. Li and Fu-wu Zhang and P. Wang},
  journal={Biochemistry (Moscow)},
  • J. Li, Cai-luan Huang, +4 authors P. Wang
  • Published 2010
  • Medicine, Chemistry
  • Biochemistry (Moscow)
  • O-GlcNAcase (OGA) is a family 84 glycoside hydrolase catalyzing the hydrolytic cleavage of O-linked β-N-acetylglucosamine (O-GlcNAc) from serine and threonine residues of proteins. Thus far, three forms of OGA have been identified in humans. Here we optimized the expression of these isoforms in E. coli and characterized their kinetic properties. Using Geno 3D, we predicted that N-terminal amino acids 63–342 form the catalytic site for O-GlcNAc removal and characterized it. Large differences are… CONTINUE READING
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    Publications referenced by this paper.
    Dynamic O-Glycosylation of Nuclear and Cytosolic Proteins
    • 261
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